HMGN3_HUMAN
ID HMGN3_HUMAN Reviewed; 99 AA.
AC Q15651; B2RD37; Q5HYD3; Q7RTT0; Q969M5; Q9BZT7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=High mobility group nucleosome-binding domain-containing protein 3;
DE AltName: Full=Thyroid receptor-interacting protein 7;
DE Short=TR-interacting protein 7;
DE Short=TRIP-7;
GN Name=HMGN3; Synonyms=TRIP7; ORFNames=PNAS-24;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH THYROID RECEPTOR,
RP AND TISSUE SPECIFICITY.
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12033773; DOI=10.1006/viro.2002.1353;
RA Leong P.W., Liew K., Lim W., Chow V.T.K.;
RT "Differential display RT-PCR analysis of enterovirus-71-infected
RT rhabdomyosarcoma cells reveals mRNA expression responses of multiple human
RT genes with known and novel functions.";
RL Virology 295:147-159(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Go V.S., Pogo B.G.T.;
RT "Identification and characterization of an estrogen inducible TRIP7-like
RT mRNA isolated by differential display.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-99 (ISOFORM 1).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP ALTERNATIVE SPLICING, INTERACTION WITH NUCLEOSOMES, AND TISSUE SPECIFICITY.
RX PubMed=11356838; DOI=10.1074/jbc.m101692200;
RA West K.L., Ito Y., Birger Y., Postnikov Y., Shirakawa H., Bustin M.;
RT "HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression
RT pattern, expand the cellular repertoire of nucleosome-binding proteins.";
RL J. Biol. Chem. 276:25959-25969(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-10 AND SER-78, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-10 AND SER-78, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH SEHBP.
RX PubMed=33468658; DOI=10.1073/pnas.2021943118;
RA Koh M., Ahmad I., Ko Y., Zhang Y., Martinez T.F., Diedrich J.K., Chu Q.,
RA Moresco J.J., Erb M.A., Saghatelian A., Schultz P.G., Bollong M.J.;
RT "A short ORF-encoded transcriptional regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Binds to nucleosomes, regulating chromatin structure and
CC consequently, chromatin-dependent processes such as transcription, DNA
CC replication and DNA repair. Affects both insulin and glucagon levels
CC and modulates the expression of pancreatic genes involved in insulin
CC secretion. Regulates the expression of the glucose transporter SLC2A2
CC by binding specifically to its promoter region and recruiting PDX1 and
CC additional transcription factors. Regulates the expression of SLC6A9, a
CC glycine transporter which regulates the glycine concentration in
CC synaptic junctions in the central nervous system, by binding to its
CC transcription start site. May play a role in ocular development and
CC astrocyte function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the ligand binding domain of the thyroid
CC receptor (TR) (in vitro) (PubMed:7776974). Requires the presence of
CC thyroid hormone for its interaction (PubMed:7776974). Interacts with
CC transcriptional regulator SEHBP (PubMed:33468658). Interacts with
CC nucleosomes (PubMed:11356838). {ECO:0000269|PubMed:11356838,
CC ECO:0000269|PubMed:33468658, ECO:0000269|PubMed:7776974}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=HMGN3a;
CC IsoId=Q15651-1; Sequence=Displayed;
CC Name=2; Synonyms=HMGN3b;
CC IsoId=Q15651-2; Sequence=VSP_017907, VSP_017908;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung, pancreas, testis,
CC skeletal muscle, heart, thyroid gland, pituitary gland, prostate and
CC uterus. Low expression in liver, spleen, placenta and ovaries.
CC {ECO:0000269|PubMed:11356838, ECO:0000269|PubMed:7776974}.
CC -!- INDUCTION: By estrogen.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L40357; AAA73877.1; ALT_INIT; mRNA.
DR EMBL; AF401520; AAK92012.1; -; mRNA.
DR EMBL; AF274949; AAK07526.1; -; mRNA.
DR EMBL; AY043282; AAK85736.1; -; mRNA.
DR EMBL; AK315391; BAG37784.1; -; mRNA.
DR EMBL; AL355796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48711.1; -; Genomic_DNA.
DR EMBL; BC009529; AAH09529.1; -; mRNA.
DR EMBL; BK000003; DAA00392.1; -; mRNA.
DR EMBL; BK000006; DAA00395.1; -; mRNA.
DR EMBL; BX648085; CAI46267.1; -; Transcribed_RNA.
DR CCDS; CCDS4988.1; -. [Q15651-1]
DR CCDS; CCDS4989.1; -. [Q15651-2]
DR RefSeq; NP_001188291.1; NM_001201362.1.
DR RefSeq; NP_001188292.1; NM_001201363.1.
DR RefSeq; NP_001305813.1; NM_001318884.1.
DR RefSeq; NP_001305814.1; NM_001318885.1.
DR RefSeq; NP_001305815.1; NM_001318886.1.
DR RefSeq; NP_001305816.1; NM_001318887.1.
DR RefSeq; NP_001305817.1; NM_001318888.1.
DR RefSeq; NP_004233.1; NM_004242.3. [Q15651-1]
DR RefSeq; NP_620058.1; NM_138730.2. [Q15651-2]
DR AlphaFoldDB; Q15651; -.
DR BioGRID; 114734; 61.
DR IntAct; Q15651; 23.
DR iPTMnet; Q15651; -.
DR PhosphoSitePlus; Q15651; -.
DR BioMuta; HMGN3; -.
DR DMDM; 23831169; -.
DR EPD; Q15651; -.
DR jPOST; Q15651; -.
DR MassIVE; Q15651; -.
DR MaxQB; Q15651; -.
DR PaxDb; Q15651; -.
DR PeptideAtlas; Q15651; -.
DR PRIDE; Q15651; -.
DR ProteomicsDB; 60689; -. [Q15651-1]
DR ProteomicsDB; 60690; -. [Q15651-2]
DR TopDownProteomics; Q15651-1; -. [Q15651-1]
DR TopDownProteomics; Q15651-2; -. [Q15651-2]
DR Antibodypedia; 3656; 172 antibodies from 24 providers.
DR DNASU; 9324; -.
DR Ensembl; ENST00000275036.11; ENSP00000275036.7; ENSG00000118418.14. [Q15651-2]
DR Ensembl; ENST00000344726.9; ENSP00000341267.5; ENSG00000118418.14. [Q15651-1]
DR GeneID; 9324; -.
DR KEGG; hsa:9324; -.
DR UCSC; uc003pis.4; human. [Q15651-1]
DR CTD; 9324; -.
DR DisGeNET; 9324; -.
DR GeneCards; HMGN3; -.
DR HGNC; HGNC:12312; HMGN3.
DR HPA; ENSG00000118418; Low tissue specificity.
DR MIM; 604502; gene.
DR neXtProt; NX_Q15651; -.
DR OpenTargets; ENSG00000118418; -.
DR PharmGKB; PA36990; -.
DR VEuPathDB; HostDB:ENSG00000118418; -.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_2_2_1; -.
DR InParanoid; Q15651; -.
DR OMA; TKAEGIC; -.
DR OrthoDB; 1617797at2759; -.
DR PhylomeDB; Q15651; -.
DR PathwayCommons; Q15651; -.
DR SignaLink; Q15651; -.
DR BioGRID-ORCS; 9324; 7 hits in 1046 CRISPR screens.
DR ChiTaRS; HMGN3; human.
DR GeneWiki; HMGN3; -.
DR GenomeRNAi; 9324; -.
DR Pharos; Q15651; Tbio.
DR PRO; PR:Q15651; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15651; protein.
DR Bgee; ENSG00000118418; Expressed in bronchial epithelial cell and 210 other tissues.
DR ExpressionAtlas; Q15651; baseline and differential.
DR Genevisible; Q15651; HS.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; NAS:UniProtKB.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:InterPro.
DR InterPro; IPR031073; HMGN3.
DR InterPro; IPR000079; HMGN_fam.
DR PANTHER; PTHR23087:SF2; PTHR23087:SF2; 1.
DR Pfam; PF01101; HMG14_17; 1.
DR PRINTS; PR00925; NONHISHMG17.
DR SMART; SM00527; HMG17; 1.
DR PROSITE; PS00355; HMG14_17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..99
FT /note="High mobility group nucleosome-binding domain-
FT containing protein 3"
FT /id="PRO_0000232574"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 76..77
FT /note="AP -> EN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12033773,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_017907"
FT VAR_SEQ 78..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12033773,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_017908"
SQ SEQUENCE 99 AA; 10666 MW; ACC44835523B9C21 CRC64;
MPKRKSPENT EGKDGSKVTK QEPTRRSARL SAKPAPPKPE PKPRKTSAKK EPGAKISRGA
KGKKEEKQEA GKEGTAPSEN GETKAEEAQK TESVDNEGE
